2CF4

Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shell

2CF4 の概要

• エントリーDOI: 10.2210/pdb2cf4/pdb
• 分子名称: PROTEIN PH0519, COBALT (II) ION (2 entities in total)
• 機能のキーワード: aminopeptidase, metalloprotein, hyperthermophile, archaea, tetrahedral, hydrolase
• 由来する生物種: PYROCOCCUS HORIKOSHII
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37324.95

構造登録者

Vellieux, F.M.D.,Schoehn, G.,Dura, M.A.,Roussel, A.,Franzetti, B. (登録日: 2006-02-15, 公開日: 2006-09-14, 最終更新日: 2024-11-06)

主引用文献

Schoehn, G.,Vellieux, F.M.D.,Dura, M.A.,Receveur-Brechot, V.,Fabry, C.M.S.,Ruigrok, R.W.H.,Ebel, C.,Roussel, A.,Franzetti, B.
An Archaeal Peptidase Assembles Into Two Different Quaternary Structures: A Tetrahedron and a Giant Octahedron.
J.Biol.Chem., 281:36327-, 2006

PubMed Abstract: Cellular proteolysis involves large oligomeric peptidases that play key roles in the regulation of many cellular processes. The cobalt-activated peptidase TET1 from the hyperthermophilic Archaea Pyrococcus horikoshii (PhTET1) was found to assemble as a 12-subunit tetrahedron and as a 24-subunit octahedral particle. Both quaternary structures were solved by combining x-ray crystallography and cryoelectron microscopy data. The internal organization of the PhTET1 particles reveals highly self-compartmentalized systems made of networks of access channels extended by vast catalytic chambers. The two edifices display aminopeptidase activity, and their organizations indicate substrate navigation mechanisms different from those described in other large peptidase complexes. Compared with the tetrahedron, the octahedron forms a more expanded hollow structure, representing a new type of giant peptidase complex. PhTET1 assembles into two different quaternary structures because of quasi-equivalent contacts that previously have only been identified in viral capsids.

PubMed: 16973604
DOI: 10.1074/JBC.M604417200

実験手法

X-RAY DIFFRACTION (3.08 Å)